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NADP

NADP, or nicotinamide adenine dinucleotide phosphate, is a crucial cofactor involved in numerous metabolic processes within living organisms.
It serves as an electron carrier, participating in redox reactions that power cellular functions.
NADP plays a central role in anabolic pathways, such as lipogenesis and biosynthesis of amino acids and nucleic acids.
It is also essential for the proper functioning of enzymes involved in antioxidant defenses, helping to maintain cellular homeostasis.
Reasearchers studying NADP-dependent processes can leverge PubCompare.ai's AI-driven platform to optimize their research, easily locate relevant protocols, and enhance the reproducibility and accuracy of their NADP studies.

Most cited protocols related to «NADP»

1
Stoichiometric Matrix and Flux Balance Analysis
A stoichiometric matrix, S (m × n), is constructed where m is the number of metabolites and n the number of reactions. Each column of S specifies the stoichiometry of the metabolites in a given reaction from the metabolic network. Mass balance equations can be written for each metabolite by taking the dot product of a row in S, corresponding to a particular metabolite, and a vector, v, containing the values of the fluxes through all reactions in the network. A system of mass balance equations for all the metabolites can be represented as follows:
where X is a concentration vector of length m, and v is a flux vector of length n. At steady-state, the time derivatives of metabolite concentrations are zero, and equation (1) can be simplified to:
S • v = 0
It follows that in order for a flux vector v to satisfy this relationship, the rate of production must equal the rate of consumption for each metabolite. Application of additional constraints further reduces the number of allowable flux distributions, v.
Limits on the range of individual flux values can further reduce the number of allowable solutions. These constraints have the form:
α ≤ vi≤ β
where α and β are the lower and upper limits, respectively. Maximum flux values (β) can be estimated based on enzymatic capacity limitations or, for the case of exchange reactions, measured maximal uptake rates can be used. Thermodynamic constraints, regarding the reversibility or irreversibility of a reaction, can be applied by setting the α for the corresponding flux to zero if the reaction is irreversible.
These constraints are not sufficient to shrink the original solution space to a single solution. Instead a number of solutions remain which make up the allowable solution space. Linear optimization can be used to find the solution that maximizes a particular objective function. Some examples of objective functions include the production of ATP, NADH, NADPH or a particular metabolite. An objective function with a combination of the metabolic precursors, energy and redox potential required for the production of biomass has proven useful in predicting in vivo cellular behavior [9 (link),10 (link),25 (link),26 ].
Reed J.L., Vo T.D., Schilling C.H, & Palsson B.O. (2003). An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR). Genome Biology, 4(9), R54.
Publication 2003
Cells Cloning Vectors derivatives Enzymes Metabolic Networks NADH NADP Oxidation-Reduction
2
Molecular Dynamics Simulation of Protein-Ligand Complexes

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Publication 2016
Cuboid Bone dihydrofolate Diphosphates Electrostatics Friction glucosyltransferase D Halogens Homo sapiens Hydrogen Hydrogen Bonds inhibitors Ligands Mitogen-Activated Protein Kinase 10 NADP NADPH Dehydrogenase Oxidoreductase Pressure Proteins Sodium Chloride Staphylococcus aureus Tetrahydrofolate Dehydrogenase Thrombin Thymidine
3
Evaluation of Watermelon Reference Genes
A total of 15 candidate reference genes were evaluated. These genes were chosen based on their previous use in watermelon or their validation as best reference genes in other crops, including 18S ribosomal RNA (18SrRNA), β-actin (ACT), clathrin adaptor complex subunit (CAC), elongation factor 1-α (EF1α), glyceraldehy-3-phosphate-dehydrogenase (GAPDH), NADP-isocitrate dehydrogenase (IDH), leunig (LUG), protein phosphatase 2A regulatory subunit A (PP2A), polypyrimidine tract-binding protein 1 (PTB), ribosomal protein S (RPS2), SAND family protein (SAND), α-tubulin (TUA), ubiquitin-conjugating enzyme E2 (UBC2), ubiquitin carrier protein (UBCP), and yellow-leaf-specific proein8 (YLS8).
For each candidate reference gene, blastn was carried out in the Cucurbit Genomics Database (http://www.icugi.org) against watermelon coding DNA sequences (CDS) (v1) using Arabidopsis homolog as a query. The CDS of the best hit was retrieved and uploaded to Primer3Plus (http://primer3plus.com/cgi-bin/dev/primer3plus.cgi) for primer design. The product size was set at the range of 80 bp to 150 bp. The forward and reverse primers were intentionally targeted on the adjoining exons, which were separated by an intron. The generated primer pair for each gene was then aligned against all watermelon CDS to confirm its specificity in silico. The specificity of the PCR amplification product for each primer pair was further determined by electrophoresis in 2% agarose gel and melting curve analysis. Finally, the watermelon species name abbreviation of ‘Cl’ was added as a prefix to the specificity-validated gene to specify the watermelon orthologous gene. For more comparable results, the primer pair of 18SrRNA, which was previously published, was used in this study [2] (link). Data on the selected reference genes and their amplification characters are listed in Table 1.
Kong Q., Yuan J., Gao L., Zhao S., Jiang W., Huang Y, & Bie Z. (2014). Identification of Suitable Reference Genes for Gene Expression Normalization in qRT-PCR Analysis in Watermelon. PLoS ONE, 9(2), e90612.
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Publication 2014
Actins Agricultural Crops alpha-Tubulin Arabidopsis Character Clathrin Adaptors EEF1A2 protein, human Electrophoresis Exons Genes Genes, vif Introns Isocitrate Dehydrogenase (NAD+) Isocitrates NADP NADPH Dehydrogenase Oligonucleotide Primers Open Reading Frames Oxidoreductase Phosphates Phosphoric Monoester Hydrolases Plant Leaves Polypyrimidine Tract-Binding Protein PPP2R4 protein, human Protein S Proteins Protein Subunits Ribosomes RNA, Ribosomal, 18S Sepharose Staphylococcal Protein A Ubiquitin-Conjugating Enzymes Watermelon
4
Quantitative Metabolic Flux Analysis
Cells were grown in Dulbecco's modified eagle media (DMEM) without pyruvate (CELLGRO) with 10% dialyzed fetal bovine serum (Invitrogen) in 5% CO2 at 37°C and harvested at ∼80% confluency. Stable knockdown cell lines were generated by shRNA-expressing lentivirus with puromycin selection. IDH1, IDH2 and ALDH1L2 knockdown was generated by transfecting cells with siRNA. For confirmation of knockdown, see Extended Figure 10. For metabolite measurements, metabolism was quenched and metabolites extracted by aspirating media and immediately adding -80°C 80:20 methanol:water. Supernatants from two rounds of extraction were combined, dried under N2, resuspended in water, placed in 4°C autosampler, and analyzed within 6 h by reversed-phase ion-pairing chromatography negative-mode electrospray-ionization high-resolution MS on a stand-alone orbitrap (Thermo)6 (link). Fluxes from 14C-labeled substrates to CO2 were measured by adding trace 14C-labeled nutrient to normal culture media, quantifying radioactive CO2 release14 (link), and correcting for intracellular substrate labeling according to percentage of radioactive tracer in the media and fraction of particular intracellular metabolite deriving from media uptake, as measured using 13C-tracer. To assess the potential contribution of various metabolic pathways to NADPH production, we analyzed feasible steady-state fluxes of a genome-scale human metabolic network model12 (link) constrained by experimentally measured uptake and excretion fluxes and growth rate of the iBMK cell line. The flux balance equations were solved in MATLAB with the objective function formulated to minimize the total sum of fluxes14 (link). NADPH consumption by reductive biosynthesis was determined based on reaction stoichiometries, experimentally measured cellular biomass composition, growth rate, fractional de novo synthesis of fatty acids (by 13C-labeling from U-13C-glucose and U-13C-glutamine), and fractional synthesis of proline from glutamate versus arginine (by 13C-labeling from U-13C-glutamine). Correction for the deuterium kinetic isotope effect was based on the assumption that total metabolic fluxes are not impacted. Let x be the fractional labeling of the relevant substrate hydrogen, FU be the NADPH production flux from unlabeled substrate and FL be the NADPH production flux from the labeled substrate.
FL/x is the flux in cases without a discernible kinetic isotope effect (e.g., for 13C). The remaining term is the correction factor for the kinetic isotope effect:
Fan J., Ye J., Kamphorst J.J., Shlomi T., Thompson C.B, & Rabinowitz J.D. (2014). Quantitative flux analysis reveals folate-dependent NADPH production. Nature, 510(7504), 298-302.
Publication 2014
Anabolism Arginine Cell Lines Cells Chromatography, Reverse-Phase Culture Media Deuterium Eagle Fatty Acids Fetal Bovine Serum Genome, Human Glucose Glutamate Glutamine Hydrogen IDH2, human Isotopes Kinetics Lentivirus Metabolic Networks Metabolism Methanol NADP Proline Protoplasm Puromycin Pyruvate Radioactive Tracers Radioactivity RNA, Small Interfering Short Hairpin RNA Trace Elements
5
Antioxidant Enzyme Activities Assay
Fresh samples (1.0 g) from control and treated seedlings were homogenized in 10 ml of chilled 50 mM potassium phosphate buffer (pH 7.0) containing 1 mM EDTA and 1% (w/v) polyvinylpyrrolidone in mortar and pestle under cool conditions. In the case of APX and DHAR activities, 1 mM ascorbic acid and 2 mM 2-mercaptoethanol were added into the above buffer, respectively. The homogenate was centrifuged at 20,000 g for 10 min at 4°C and supernatant was used as an enzyme. All enzymatic measurements were carried out at 25°C by using a Shimadzu, UV-VIS Spectrophotometer (UV-1700 Pharma Spec) (Gangwar et al., 2011 (link)).
APX (EC 1.11.1.11) activity was determined according to the method of Nakano and Asada (1981) . The decrease in absorbance was measured at 290 nm. The enzyme activity was calculated by using an extinction coefficient of 2.8 mM-1 cm-1. One unit (U) of enzyme activity is defined as 1 nmol ascorbate oxidized min-1.
Glutathione reductase (EC 1.6.4.2) activity was assayed according to the method of Schaedle and Bassham (1977) (link). The decrease in absorbance was read at 340 nm, and GR activity was calculated using an extinction coefficient of 6.2 mM-1 cm-1. One unit (U) of enzyme activity is defined as 1 nmol NADPH oxidized min-1.
Monodehydroascorbate reductase (EC 1.6.5.4) activity was estimated according to the method of Hossain et al. (1984) . The enzyme activity was calculated using an extinction coefficient of 6.2 mM-1 cm-1. One unit (U) of enzyme activity is defined as nmol NADPH oxidized min-1.
Dehydroascorbate reductase (EC 1.8.5.1) activity was assayed by the method of Nakano and Asada (1981) . An increase in absorbance was read at 265 nm, and DHAR activity was calculated using an extinction coefficient of 7.0 mM-1 cm-1. One unit (U) of enzyme activity is defined as 1 nmol DHA reduced min-1.
Tripathi D.K., Mishra R.K., Singh S., Singh S., Vishwakarma K., Sharma S., Singh V.P., Singh P.K., Prasad S.M., Dubey N.K., Pandey A.C., Sahi S, & Chauhan D.K. (2017). Nitric Oxide Ameliorates Zinc Oxide Nanoparticles Phytotoxicity in Wheat Seedlings: Implication of the Ascorbate–Glutathione Cycle. Frontiers in Plant Science, 8, 1.
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Publication 2017
2-Mercaptoethanol AFR reductase Ascorbic Acid Buffers dehydroascorbate reductase Edetic Acid enzyme activity Enzymes Extinction, Psychological Glutathione Reductase NADP Phosphates Potassium-50 Povidone Seedlings

Most recents protocols related to «NADP»

1
Biosynthesis of Bisbenzylisoquinoline Alkaloids in Engineered Yeast
Not available on PMC !

Example 5

FIG. 16 illustrates (A) a biosynthetic scheme for conversion of L-tyrosine to bisBlAs and (B) yeast strains engineered to biosynthesize bisBlAs, in accordance with embodiments of the invention. In particular, FIG. 16 illustrates (A) a pathway that is used to produce bisBlAs berbamunine and guattegaumerine. FIG. 16 provides the use of the enzymes ARO9, aromatic aminotransferase; ARO10, phenylpyruvate decarboxlase; TyrH, tyrosine hydroxylase; DODC, DOPA decarboxylase; NCS, norcoclaurine synthase; 6OMT, 6-O-methyltransferase; CNMT, coclaurine N-methyltransferase; CYP80A1, cytochrome P450 80A1; CPR, cytochrome P450 NADPH reductase. Of the metabolites provided in FIG. 16, 4-HPA, 4-HPP, and L-tyrosine are naturally synthesized in yeast. Other metabolites that are shown in FIG. 16 are not naturally produced in yeast.

In examples of the invention, a bisBIA-producing yeast strain, that produces bisBlAs such as those generated using the pathway illustrated in (A), is engineered by integration of a single construct into locus YDR514C. Additionally, FIG. 16 provides (B) example yeast strains engineered to synthesize bisBlAs. Ps6OMT, PsCNMT, PsCPR, and BsCYP80A1 were integrated into the yeast genome at a single locus (YDR514C). Each enzyme was expressed from a constitutive promoter. The arrangement and orientation of gene expression cassettes is indicated by arrows in the schematic. These strains convert (R)- and (S)-norcoclaurine to coclaurine and then to N-methylcoclaurine. In one example, the strains may then conjugate one molecule of (R)—N-methylcoclaurine and one molecule of (S)—N-methylcoclaurine to form berbamunine. In another example, the strains may conjugate two molecules of (R)—N-methylcoclaurine to form guattegaumerine. In another example, the strains may conjugate one molecule of (R)—N-methylcoclaurine and one molecule of (S)-coclaurine to form 2′-norberbamunine. In another embodiment, the strain may be engineered to supply the precursors (R)- and (S)-norcoclaurine from L-tyrosine, as provided in FIG. 5.

The construct includes expression cassettes for P. somniferum enzymes 6OMT and CNMT expressed as their native plant nucleotide sequences. A third enzyme from P. somniferum, CPR, is codon optimized for expression in yeast. The PsCPR supports the activity of a fourth enzyme, Berberis stolonifera CYP80A1, also codon optimized for expression in yeast. The expression cassettes each include unique yeast constitutive promoters and terminators. Finally, the integration construct includes a LEU2 selection marker flanked by loxP sites for excision by Cre recombinase.

A yeast strain expressing Ps6OMT, PsCNMT, BsCYP80A1, and PsCPR is cultured in selective medium for 16 hours at 30° C. with shaking. Cells are harvested by centrifugation and resuspended in 400 μL breaking buffer (100 mM Tris-HCl, pH 7.0, 10% glycerol, 14 mM 2-mercaptoethanol, protease inhibitor cocktail). Cells are physically disrupted by the addition of glass beads and vortexing. The liquid is removed and the following substrates and cofactors are added to start the reaction: 1 mM (R,S)-norcoclaurine, 10 mM S-adenosyl methionine, 25 mM NADPH. The crude cell lysate is incubated at 30° C. for 4 hours and then quenched by the 1:1 addition of ethanol acidified with 0.1% acetic acid. The reaction is centrifuged and the supernatant analyzed by liquid chromatography mass spectrometry (LC-MS) to detect bisBlA products berbamunine, guattegaumerine, and 2′-norberbamunine by their retention and mass/charge.

US11859225B2. Methods of producing epimerases and benzylisoquinoline alkaloids (2024-01-02). The Board of Trustees of the Leland Stanford Junior University [US]. Inventors: Christina D. Smolke [US], Stephanie Galanie [US], Isis Trenchard [US], Catherine Thodey [US], Yanran Li [US].
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Patent 2024
2-Mercaptoethanol 3-phenylpyruvate Acetic Acid Allopurinol Anabolism Barberry Base Sequence berbamunine Buffers Cells Centrifugation coclaurine Codon Cre recombinase Culture Media Cytochrome P450 Dopa Decarboxylase enzyme activity Enzymes Ethanol Gene Expression Genome Glycerin guatteguamerine higenamine Liquid Chromatography Mass Spectrometry Methyltransferase NADP NADPH-Ferrihemoprotein Reductase norcoclaurine synthase Plants Protease Inhibitors Retention (Psychology) S-adenosyl-L-methionine coclaurine N-methyltransferase S-Adenosylmethionine Saccharomyces cerevisiae Strains Transaminases Tromethamine Tyrosine Tyrosine 3-Monooxygenase
2
Metabolic Enzyme Activities in Rice
Activities of enzymes related to C metabolism, including PEPC (Osuna et al., 1996 (link)),ERS (Ratinaud et al., 1983 (link)), TPS (Goddijn et al., 1997 (link)), and SPS (Feng et al., 2019 (link)) in rice tissues were assayed (detailed information is shown in Supplementary material M1).
Activities of enzymes activated in N metabolism, namely, NR (Ahanger et al., 2021 (link)), nitrite reductase (NiR) (Lin et al., 2022a (link)), and GS (Hou et al., 2019 (link)) in rice tissues were determined (detailed information is shown in Supplementary material M1).
Activities of enzymes involved in 2-OG biosynthesis, i.e., NADP-ICDH (Gálvez et al., 1994 (link)), isocitrate dehydrogenases (NAD-IDH) (Gálvez et al., 1994 (link)), and glutamate dehydrogenases (GDH) (Turano et al., 1996 (link)), were also measured (detailed information is shown in Supplementary material M1).
Feng Y.X., Yang L., Lin Y.J., Song Y, & Yu X.Z. (2023). Merging the occurrence possibility into gene co-expression network deciphers the importance of exogenous 2-oxoglutarate in improving the growth of rice seedlings under thiocyanate stress. Frontiers in Plant Science, 14, 1086098.
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Publication 2023
Anabolism enzyme activity Glutamate Dehydrogenase Isocitrate Dehydrogenase (NAD+) Metabolism NADP Nitrite Reductase Oryza sativa Tissues
3
Quantifying CNM-related Enzymes in Rice
Real-time quantitative PCR (RT-qPCR) was used to quantify the expression levels of CNM-related enzymes in rice seedlings after SCN− exposure. Total RNA was extracted from both the root and shoot of all rice samples by using an Ultrapure RNA Kit (CWBio, Taizhou, China). DNase I (CWBio, Taizhou, China) was used to remove genomic DNA contamination, if any, from RNA extract. Then, the total RNA was purified by an RNeasy MinElute Cleanup Kit (Qiagen, Hilden, Germany). Each sample was prepared in four independent biological replicates.
A total of 40 genes encoding enzymes or proteins activated in the CNM pathways were searched from the databases, including RGAP (http://rice.plantbiology.msu.edu/analyses_search_blast.shtml), NCBI (https://www.ncbi.nlm.nih.gov/), and RAPDB (http://rapdb.dna.affrc.go.jp/). Expression of genes was assayed after SCN− exposure by RT-qPCR analysis, including PEPC (Osppc1, Osppc2a, Osppc3, and Osppc4), ERS (OsERS1, OsERS2, and OsERS3), TPS (OsTPS1, OsTPS4, OsTPS5, OsTPS8, and OsTPS9), SPS (OsSPS1, OsSPS2, OsSPS4, OsSPS5, and OsSPS6), NR (OsNIA1, OsNIA2, and OsNR1), NiR (OsNiR1, OsNiR2, and OsNiR3), GS (OsGS1;1, OsGS1;2, OsGS1;3, and OsGS2), NADP-ICDH (OsICDH1, OsICDH2, OsICDH3, and OsICDH4), NAD-IDH (OsIDHc;2, OsIDHc;1, OsIDHa, and OsIDH1), and GDH (OsGDH1, OsGDH2, OsGDH3, and OsGDH4). All genes primer sequences are listed in Table S1. RT-qPCR cycling conditions were as follows: 1) denaturation at 95°C for 10 s, 2) annealing at 58°C for 30 s, and 3) extension at 72°C for 32 s. This cycle was imitated 40 times. The RT-qPCR analysis was executed using the 7500 Fast Real-Time PCR system (Applied Biosystems, Foster City, CA, USA) and SYBR green chemistry. Rice GAPDH (glyceraldehyde-3-phosphate dehydrogenase, LOC_Os08g03290.1) was selected as the housekeeping gene (Yang et al., 2021 (link)). The standard 2−ΔΔCT method was used to calculate the relative expression of each of the targeted genes (Schmittgen and Livak, 2008 (link)). All values were represented as cumulative means ± standard deviation of four independent replicates.
Feng Y.X., Yang L., Lin Y.J., Song Y, & Yu X.Z. (2023). Merging the occurrence possibility into gene co-expression network deciphers the importance of exogenous 2-oxoglutarate in improving the growth of rice seedlings under thiocyanate stress. Frontiers in Plant Science, 14, 1086098.
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Publication 2023
Biopharmaceuticals Deoxyribonuclease I DNA Contamination Enzymes GAPDH protein, human Gene Expression Genes Genes, Housekeeping Genes, vif Genome Glyceraldehyde-3-Phosphate Dehydrogenases NADP Oligonucleotide Primers Oryza sativa Plant Roots Proteins Real-Time Polymerase Chain Reaction rGAP Seedlings SYBR Green I Test, Clinical Enzyme
4
Measuring Intracellular NADPH Levels
Intracellular NADPH concentrations were measured using the Enzychrom NADP/NADPH assay kit (BioAssay Systems) according to the manufacturer’s protocol.
Jiang M., Su Y.B., Ye J.Z., Li H., Kuang S.F., Wu J.H., Li S.H., Peng X.X, & Peng B. (2023). Ampicillin-controlled glucose metabolism manipulates the transition from tolerance to resistance in bacteria. Science Advances, 9(10), eade8582.
Publication 2023
Biological Assay NADP Protoplasm
5
Metabolic Stability Determination Using Hepatic Microsomes
The metabolic stability of test compounds was determined as described.57 (link),58 (link) Incubation and experimental conditions with human hepatic microsomal fractions (purchased from BD Gentest as a pooled batch from 6 donors) were as follows: microsomal proteins, 1 mg/mL; bovine serum albumin, 1 mg/mL; substrate, 5 μM; incubation duration, 20 min; cytochrome P-450 monooxygenases (CYPs) and flavin containing monooxygenases (FMOs) cofactor, 1 mM NADPH. Enzyme activity was stopped with 1 volume of acetonitrile. Ketoconazole at a final concentration of 1.5 μM (100-fold above its Ki for CYP3A4) was used for the specific and potent inhibition of enzyme reactions catalyzed by CYP3A4. For each test compound and for each microsomal preparation, three incubations were prepared: absolute reference in buffer (without enzyme material, i.e., microsomes); incubation without NADPH cofactor (with microsomal fractions); and incubation with NADPH (with microsomal fractions). For most compounds, biotransformation, as observed in hepatic microsomal fractions in the presence of the NADPH cofactor, consists of oxidative reactions catalyzed by either CYPs or FMOs. In these conditions, the percentage of total metabolism, which corresponds to oxidative metabolism, was determined as follows: [% total metabolism] ≈ [% oxidative metabolism] = [unchanged compound (UC) peak area − NADPH UC peak area + NADPH] × 100%, where NADPH corresponds to the enzyme cofactor for oxidation reactions catalyzed by either CYP or FMO.
Zhang J., Lair C., Roubert C., Amaning K., Barrio M.B., Benedetti Y., Cui Z., Xing Z., Li X., Franzblau S.G., Baurin N., Bordon-Pallier F., Cantalloube C., Sans S., Silve S., Blanc I., Fraisse L., Rak A., Jenner L.B., Yusupova G., Yusupov M., Zhang J., Kaneko T., Yang T.J., Fotouhi N., Nuermberger E., Tyagi S., Betoudji F., Upton A., Sacchettini J.C, & Lagrange S. (2023). Discovery of natural-product-derived sequanamycins as potent oral anti-tuberculosis agents. Cell, 186(5), 1013-1025.e24.
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Publication 2023
acetonitrile Biotransformation Buffers Cell Respiration Coenzymes Cytochrome P-450 CYP3A4 Cytochrome P-450 Monooxygenase dimethylaniline monooxygenase (N-oxide forming) Donors enzyme activity Enzymes Homo sapiens Ketoconazole Liver Diseases Metabolism Microsomes NADP Proteins Serum Albumin, Bovine

Top products related to «NADP»

1
Nadph by Merck Group
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NADPH, or Nicotinamide Adenine Dinucleotide Phosphate, is a cofactor essential for various cellular processes. It plays a crucial role in enzymatic reactions, serving as an electron donor in oxidation-reduction reactions. NADPH is a key component in several metabolic pathways, including biosynthesis, antioxidant defense, and energy production.
2
Glucose 6 phosphate (g6p) by Merck Group
Sourced in United States, Germany, China, United Kingdom, France, Canada, Australia, Spain, Switzerland
Glucose-6-phosphate is a chemical compound that plays a crucial role in cellular metabolism. It is an intermediate in the glycolysis pathway, which is the process of breaking down glucose to generate energy for the cell. Glucose-6-phosphate is the product of the first step in glycolysis, where glucose is phosphorylated by the enzyme hexokinase. This compound is a key component in various biochemical processes, including energy production, glucose storage, and the pentose phosphate pathway.
3
Glucose 6 phosphate dehydrogenase by Merck Group
Sourced in United States, Germany, China, Canada, Macao, Australia, Sao Tome and Principe
Glucose-6-phosphate dehydrogenase is an enzyme that catalyzes the conversion of glucose-6-phosphate to 6-phosphoglucono-δ-lactone, the first step of the pentose phosphate pathway. This enzyme plays a crucial role in maintaining cellular redox balance and generating NADPH, which is essential for various cellular processes.
4
Bovine serum albumin (bsa) by Merck Group
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
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Glutathione reductase by Merck Group
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Glutathione reductase is an enzyme that catalyzes the reduction of oxidized glutathione (GSSG) to its reduced form (GSH). This enzyme is involved in maintaining the balance of reduced and oxidized glutathione within cells, which is important for cellular antioxidant defense systems.
6
Dimethyl sulfoxide (dmso) by Merck Group
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
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Formic acid by Merck Group
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Formic acid is a colorless, pungent-smelling liquid chemical compound. It is the simplest carboxylic acid, with the chemical formula HCOOH. Formic acid is widely used in various industrial and laboratory applications.
9
Nadp nadph assay kit by Abcam
Sourced in United Kingdom, United States, China
The NADP/NADPH Assay Kit is a biochemical tool designed to detect and quantify the levels of the coenzymes NADP (nicotinamide adenine dinucleotide phosphate) and NADPH (the reduced form of NADP) in biological samples. The kit provides a colorimetric or fluorometric-based assay that enables the measurement of NADP and NADPH concentrations.
10
Lucigenin by Merck Group
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Lucigenin is a fluorescent compound used in analytical chemistry and biochemistry as a chemiluminescent indicator. It is commonly employed in assays for the detection and quantification of superoxide radicals.

More about "NADP"

Nicotinamide adenine dinucleotide phosphate (NADP) is a crucial cofactor involved in numerous metabolic processes within living organisms.
It serves as an electron carrier, participating in redox reactions that power cellular functions.
NADP plays a central role in anabolic pathways, such as lipogenesis and biosynthesis of amino acids and nucleic acids.
It is also essential for the proper functioning of enzymes involved in antioxidant defenses, helping to maintain cellular homeostasis.
NADPH, the reduced form of NADP, is a key player in glucose-6-phosphate dehydrogenase (G6PD) and glutathione reductase activities.
G6PD catalyzes the first step in the pentose phosphate pathway, generating NADPH, which is crucial for protecting cells against oxidative stress.
Glutathione reductase, on the other hand, utilizes NADPH to maintain the reduced state of glutathione (GSH), a vital antioxidant in the cell.
Researchers studying NADP-dependent processes can leverage PubCompare.ai's AI-driven platform to optimize their research.
This powerful tool can help locate relevant protocols from literature, preprints, and patents, and enable intelligent comparisons to identify the best protocols and products.
By using PubCompare.ai, researchers can enhance the reproducibility and accuracy of their NADP studies, ensuring their work is supported by high-quality, reliable information.
In addition to NADP, other related terms and compounds, such as DMSO, formic acid, and NADP/NADPH assay kits, can also be incorporated into the research process to provide a comprehensive understanding of the cellular mechanisms and pathways involving NADP.
By utilizing these resources and tools, researchers can gain deeper insights into the role of NADP in biological systems and advance their scientific investigations with greater efficiency and confidence.